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Q9Y657

- SPIN1_HUMAN

UniProt

Q9Y657 - SPIN1_HUMAN

Protein

Spindlin-1

Gene

SPIN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (18 Apr 2006)
      Previous versions | rss
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    Functioni

    Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway dowstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway (PubMed:24589551). Overexpression induces metaphase arrest and chromosomal instability. Localizes to active rDNA loci and promotes the expression of rRNA genes (PubMed:21960006). May play a role in cell-cycle regulation during the transition from gamete to embryo. Involved in oocyte meiotic resumption, a process that takes place before ovulation to resume meiosis of oocytes blocked in prophase I: may act by regulating maternal transcripts to control meiotic resumption.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei173 – 1731Histone H3K4me3 and H3R8me2a
    Binding sitei180 – 1801Histone H3K4me3 and H3R8me2a
    Binding sitei184 – 1841Histone H3K4me3 and H3R8me2a

    GO - Molecular functioni

    1. methylated histone binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. gamete generation Source: InterPro
    3. meiotic nuclear division Source: UniProtKB-KW
    4. multicellular organismal development Source: UniProtKB-KW
    5. positive regulation of Wnt signaling pathway Source: UniProtKB
    6. rRNA transcription Source: UniProtKB
    7. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Developmental protein

    Keywords - Biological processi

    Cell cycle, Meiosis, Wnt signaling pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Spindlin-1
    Alternative name(s):
    Ovarian cancer-related protein
    Spindlin1
    Gene namesi
    Name:SPIN1
    Synonyms:OCR, SPIN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:11243. SPIN1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleolus Source: UniProtKB
    2. nucleus Source: LIFEdb
    3. spindle Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi72 – 721W → A or R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. 1 Publication
    Mutagenesisi98 – 981Y → R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. 1 Publication
    Mutagenesisi109 – 1091S → A: Impaired phosphorylation. 1 Publication
    Mutagenesisi124 – 1241S → A: Impaired phosphorylation. 1 Publication
    Mutagenesisi141 – 1411F → A: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. Impaired ability to activate expression of pre-rRNA. 2 Publications
    Mutagenesisi142 – 1421E → A: Impaired binding to histone H3K4me3 and H3R8me2a. 1 Publication
    Mutagenesisi170 – 1701Y → A: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. Impaired ability to activate expression of pre-rRNA. 2 Publications
    Mutagenesisi177 – 1771Y → A: Impaired binding to histone H3K4me3 and H3R8me2a. 1 Publication
    Mutagenesisi184 – 1841D → A or R: Impaired binding to histone H3K4me3 and H3R8me2a. 2 Publications
    Mutagenesisi189 – 1891D → A or R: Impaired binding to histone H3K4me3. 1 Publication
    Mutagenesisi251 – 2511F → R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. 1 Publication

    Organism-specific databases

    PharmGKBiPA162404504.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 262262Spindlin-1PRO_0000181367Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei44 – 441N6-acetyllysineBy similarity
    Modified residuei109 – 1091Phosphoserine; by AURKA1 Publication
    Modified residuei124 – 1241Phosphoserine; by AURKA3 Publications
    Modified residuei199 – 1991Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated during oocyte meiotic maturation.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y657.
    PaxDbiQ9Y657.
    PRIDEiQ9Y657.

    PTM databases

    PhosphoSiteiQ9Y657.

    Expressioni

    Tissue specificityi

    Highly expressed in ovarian cancer tissues.1 Publication

    Gene expression databases

    BgeeiQ9Y657.
    CleanExiHS_SPIN1.
    GenevestigatoriQ9Y657.

    Organism-specific databases

    HPAiHPA000162.

    Interactioni

    Subunit structurei

    Homodimer; may form higher-order oligomers (PubMed:17082182). Interacts with TCF7L2/TCF4; the interaction is direct. Interacts with HABP4 and SERBP1.4 Publications

    Protein-protein interaction databases

    BioGridi116130. 15 interactions.
    DIPiDIP-40062N.
    IntActiQ9Y657. 7 interactions.
    MINTiMINT-1428826.
    STRINGi9606.ENSP00000365019.

    Structurei

    Secondary structure

    1
    262
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi56 – 627
    Beta strandi65 – 673
    Beta strandi70 – 7910
    Beta strandi87 – 915
    Beta strandi98 – 1003
    Turni102 – 1043
    Beta strandi108 – 11710
    Helixi126 – 1327
    Beta strandi136 – 1427
    Beta strandi144 – 1463
    Beta strandi148 – 15811
    Beta strandi160 – 1623
    Beta strandi166 – 1705
    Beta strandi173 – 1797
    Helixi181 – 1866
    Beta strandi190 – 1923
    Beta strandi217 – 2215
    Turni223 – 2253
    Beta strandi227 – 2359
    Beta strandi237 – 2393
    Beta strandi242 – 2476
    Beta strandi254 – 2574

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NS2X-ray2.20A/B26-262[»]
    4H75X-ray2.10A27-262[»]
    4MZFX-ray2.10B50-262[»]
    4MZGX-ray1.70B/D50-262[»]
    4MZHX-ray2.20A50-262[»]
    ProteinModelPortaliQ9Y657.
    SMRiQ9Y657. Positions 50-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y657.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 11664Tudor-like domain 1Add
    BLAST
    Regioni93 – 986Histone H3K4me3 and H3R8me2a binding
    Regioni132 – 19362Tudor-like domain 2Add
    BLAST
    Regioni142 – 1421Histone H3K4me3 and H3R8me2a binding
    Regioni213 – 26250Tudor-like domain 3Add
    BLAST
    Regioni250 – 2523Histone H3K4me3 and H3R8me2a binding

    Domaini

    The 3 tudor-like domains (also named Spin/Ssty repeats) specifically recognize and bind methylated histones (PubMed:23077255, PubMed:24589551). H3K4me3 and H3R8me2a are recognized by tudor-like domains 2 and 1, respectively (PubMed:24589551).3 Publications

    Sequence similaritiesi

    Belongs to the SPIN/STSY family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG40069.
    HOGENOMiHOG000293367.
    HOVERGENiHBG000686.
    InParanoidiQ9Y657.
    OMAiHKDERVQ.
    OrthoDBiEOG7CK37K.
    PhylomeDBiQ9Y657.
    TreeFamiTF332665.

    Family and domain databases

    InterProiIPR003671. SPIN/Ssty.
    IPR029565. Spindlin-1.
    [Graphical view]
    PANTHERiPTHR10405. PTHR10405. 1 hit.
    PTHR10405:SF15. PTHR10405:SF15. 1 hit.
    PfamiPF02513. Spin-Ssty. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y657-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTPFGKTPG QRSRADAGHA GVSANMMKKR TSHKKHRSSV GPSKPVSQPR    50
    RNIVGCRIQH GWKEGNGPVT QWKGTVLDQV PVNPSLYLIK YDGFDCVYGL 100
    ELNKDERVSA LEVLPDRVAT SRISDAHLAD TMIGKAVEHM FETEDGSKDE 150
    WRGMVLARAP VMNTWFYITY EKDPVLYMYQ LLDDYKEGDL RIMPDSNDSP 200
    PAEREPGEVV DSLVGKQVEY AKEDGSKRTG MVIHQVEAKP SVYFIKFDDD 250
    FHIYVYDLVK TS 262
    Length:262
    Mass (Da):29,601
    Last modified:April 18, 2006 - v3
    Checksum:i49F86CBCC7A0AA01
    GO

    Sequence cautioni

    The sequence AAD43035.1 differs from that shown. Reason: Frameshift at position 21.
    The sequence AAG38112.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAG48367.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAB66653.1 differs from that shown. Reason: Erroneous termination at position 171. Translated as Glu.
    The sequence CAG38515.1 differs from that shown. Reason: Erroneous termination at position 171. Translated as Glu.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti49 – 491P → S in BAG52466. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti221 – 2211A → P.
    Corresponds to variant rs34794905 [ dbSNP | Ensembl ].
    VAR_053690

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF106682 mRNA. Translation: AAD43035.1. Frameshift.
    AF087864 mRNA. Translation: AAG48367.1. Different initiation.
    AF317228 mRNA. Translation: AAG38112.1. Different initiation.
    AL136719 mRNA. Translation: CAB66653.1. Sequence problems.
    BT007314 mRNA. Translation: AAP35978.1.
    AK092017 mRNA. Translation: BAG52466.1.
    AK289691 mRNA. Translation: BAF82380.1.
    AK290009 mRNA. Translation: BAF82698.1.
    AK315854 mRNA. Translation: BAF98745.1.
    AL353748 Genomic DNA. Translation: CAH72406.1.
    CH471089 Genomic DNA. Translation: EAW62753.1.
    BC013571 mRNA. No translation available.
    BC114515 mRNA. Translation: AAI14516.1.
    BC114565 mRNA. Translation: AAI14566.1.
    CR533484 mRNA. Translation: CAG38515.1. Sequence problems.
    CCDSiCCDS43843.1.
    RefSeqiNP_006708.2. NM_006717.2.
    UniGeneiHs.146804.

    Genome annotation databases

    EnsembliENST00000375859; ENSP00000365019; ENSG00000106723.
    GeneIDi10927.
    KEGGihsa:10927.
    UCSCiuc004apy.3. human.

    Polymorphism databases

    DMDMi93141317.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF106682 mRNA. Translation: AAD43035.1 . Frameshift.
    AF087864 mRNA. Translation: AAG48367.1 . Different initiation.
    AF317228 mRNA. Translation: AAG38112.1 . Different initiation.
    AL136719 mRNA. Translation: CAB66653.1 . Sequence problems.
    BT007314 mRNA. Translation: AAP35978.1 .
    AK092017 mRNA. Translation: BAG52466.1 .
    AK289691 mRNA. Translation: BAF82380.1 .
    AK290009 mRNA. Translation: BAF82698.1 .
    AK315854 mRNA. Translation: BAF98745.1 .
    AL353748 Genomic DNA. Translation: CAH72406.1 .
    CH471089 Genomic DNA. Translation: EAW62753.1 .
    BC013571 mRNA. No translation available.
    BC114515 mRNA. Translation: AAI14516.1 .
    BC114565 mRNA. Translation: AAI14566.1 .
    CR533484 mRNA. Translation: CAG38515.1 . Sequence problems.
    CCDSi CCDS43843.1.
    RefSeqi NP_006708.2. NM_006717.2.
    UniGenei Hs.146804.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2NS2 X-ray 2.20 A/B 26-262 [» ]
    4H75 X-ray 2.10 A 27-262 [» ]
    4MZF X-ray 2.10 B 50-262 [» ]
    4MZG X-ray 1.70 B/D 50-262 [» ]
    4MZH X-ray 2.20 A 50-262 [» ]
    ProteinModelPortali Q9Y657.
    SMRi Q9Y657. Positions 50-260.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116130. 15 interactions.
    DIPi DIP-40062N.
    IntActi Q9Y657. 7 interactions.
    MINTi MINT-1428826.
    STRINGi 9606.ENSP00000365019.

    PTM databases

    PhosphoSitei Q9Y657.

    Polymorphism databases

    DMDMi 93141317.

    Proteomic databases

    MaxQBi Q9Y657.
    PaxDbi Q9Y657.
    PRIDEi Q9Y657.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375859 ; ENSP00000365019 ; ENSG00000106723 .
    GeneIDi 10927.
    KEGGi hsa:10927.
    UCSCi uc004apy.3. human.

    Organism-specific databases

    CTDi 10927.
    GeneCardsi GC09P091003.
    HGNCi HGNC:11243. SPIN1.
    HPAi HPA000162.
    MIMi 609936. gene.
    neXtProti NX_Q9Y657.
    PharmGKBi PA162404504.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40069.
    HOGENOMi HOG000293367.
    HOVERGENi HBG000686.
    InParanoidi Q9Y657.
    OMAi HKDERVQ.
    OrthoDBi EOG7CK37K.
    PhylomeDBi Q9Y657.
    TreeFami TF332665.

    Miscellaneous databases

    ChiTaRSi SPIN1. human.
    EvolutionaryTracei Q9Y657.
    GeneWikii SPIN1.
    GenomeRNAii 10927.
    NextBioi 41511.
    PROi Q9Y657.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y657.
    CleanExi HS_SPIN1.
    Genevestigatori Q9Y657.

    Family and domain databases

    InterProi IPR003671. SPIN/Ssty.
    IPR029565. Spindlin-1.
    [Graphical view ]
    PANTHERi PTHR10405. PTHR10405. 1 hit.
    PTHR10405:SF15. PTHR10405:SF15. 1 hit.
    Pfami PF02513. Spin-Ssty. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Peng Y., Song H., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., Luo M., Chen J., Hu R.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pituitary.
    2. "Cloning, characterization and mapping of human SPIN to human chromosome 9q22.1-22.3."
      Zhang H.L., Yu L., Wang X., Chen Z., Tu Q., Chen J.Q., Ding J.B., Gao J., Zhao S.Y.
      Chin. Sci. Bull. 45:909-914(2000)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Spindlin1, a novel nuclear protein with a role in the transformation of NIH3T3 cells."
      Gao Y., Yue W., Zhang P., Li L., Xie X., Yuan H., Chen L., Liu D., Yan F., Pei X.
      Biochem. Biophys. Res. Commun. 335:343-350(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
      Tissue: Ovarian carcinoma.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Fetal kidney.
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Amygdala, Hippocampus and Trachea.
    7. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Uterus.
    10. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-225.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Nucleolar protein Spindlin1 recognizes H3K4 methylation and stimulates the expression of rRNA genes."
      Wang W., Chen Z., Mao Z., Zhang H., Ding X., Chen S., Zhang X., Xu R., Zhu B.
      EMBO Rep. 12:1160-1166(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-141 AND TYR-170.
    15. "SPINDLIN1 promotes cancer cell proliferation through activation of WNT/TCF-4 signaling."
      Wang J.X., Zeng Q., Chen L., Du J.C., Yan X.L., Yuan H.F., Zhai C., Zhou J.N., Jia Y.L., Yue W., Pei X.T.
      Mol. Cancer Res. 10:326-335(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TCF7L2, PHOSPHORYLATION AT SER-109 AND SER-124, MUTAGENESIS OF SER-109 AND SER-124, TISSUE SPECIFICITY.
    16. "Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation."
      Zhao Q., Qin L., Jiang F., Wu B., Yue W., Xu F., Rong Z., Yuan H., Xie X., Gao Y., Bai C., Bartlam M., Pei X., Rao Z.
      J. Biol. Chem. 282:647-656(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-262 IN COMPLEX WITH PHOSPHATE IONS, DNA-BINDING, SUBUNIT, DOMAINS TUDOR-LIKE.
    17. "Distinct mode of methylated lysine-4 of histone H3 recognition by tandem tudor-like domains of Spindlin1."
      Yang N., Wang W., Wang Y., Wang M., Zhao Q., Rao Z., Zhu B., Xu R.M.
      Proc. Natl. Acad. Sci. U.S.A. 109:17954-17959(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 27-262 IN COMPLEX WITH METHYLATED HISTONE H3, MUTAGENESIS OF ASP-184 AND ASP-189.
    18. "Molecular basis underlying histone H3 lysine-arginine methylation pattern readout by Spin/Ssty repeats of Spindlin1."
      Su X., Zhu G., Ding X., Lee S.Y., Dou Y., Zhu B., Wu W., Li H.
      Genes Dev. 28:622-636(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 50-262 IN COMPLEX WITH METHYLATED HISTONE H3, FUNCTION, INTERACTION WITH TCF7L2, MUTAGENESIS OF TRP-72; TYR-98; PHE-141; GLU-142; TYR-170; TYR-177; ASP-184 AND PHE-251.

    Entry informationi

    Entry nameiSPIN1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y657
    Secondary accession number(s): A8K0X6
    , B3KRQ4, Q7KZJ8, Q9GZT2, Q9H0N7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: April 18, 2006
    Last modified: October 1, 2014
    This is version 107 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3